ID HPPD_PSEUJ Reviewed; 357 AA. AC P80064; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1992, sequence version 1. DT 22-JUL-2008, entry version 64. DE RecName: Full=4-hydroxyphenylpyruvate dioxygenase; DE Short=HPPDase; DE Short=4HPPD; DE Short=HPD; DE EC=1.13.11.27; GN Name=hpd; OS Pseudomonas sp. (strain P.J. 874). OC Bacteria; Proteobacteria. OX NCBI_TaxID=72587; RN [1] RP PROTEIN SEQUENCE. RX MEDLINE=92241278; PubMed=1572351; RA Rueetschi U., Odelhoeg B., Lindstedt S., Barros-Soederling J., RA Persson B., Joernvall H.; RT "Characterization of 4-hydroxyphenylpyruvate dioxygenase. Primary RT structure of the Pseudomonas enzyme."; RL Eur. J. Biochem. 205:459-466(1992). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). RX MEDLINE=99404943; PubMed=10467142; DOI=10.1016/S0969-2126(99)80124-5; RA Serre L., Sailland A., Sy D., Boudec P., Rolland A., RA Pebay-Peyroula E., Cohen-Addad C.; RT "Crystal structure of Pseudomonas fluorescens 4-hydroxyphenylpyruvate RT dioxygenase: an enzyme involved in the tyrosine degradation pathway."; RL Structure 7:977-988(1999). CC -!- CATALYTIC ACTIVITY: 4-hydroxyphenylpyruvate + O(2) = homogentisate CC + CO(2). CC -!- COFACTOR: Binds 1 iron ion per subunit. CC -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation; CC acetoacetic acid and fumarate from L-phenylalanine: step 3/6. CC -!- SUBUNIT: Homotetramer. CC -!- SIMILARITY: Belongs to the 4HPPD family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR PIR; S21209; S21209. DR PDB; 1CJX; X-ray; 2.40 A; A/B/C/D=1-357. DR PDBsum; 1CJX; -. DR BioCyc; MetaCyc:MON-12032; -. DR InterPro; IPR005956; 4OHPhenylPyrv_dOase. DR InterPro; IPR004360; Glyas_bleo-R_dOase. DR PANTHER; PTHR11959; HPP_dOase; 1. DR Pfam; PF00903; Glyoxalase; 1. DR PIRSF; PIRSF009283; HPP_dOase; 1. DR TIGRFAMs; TIGR01263; 4HPPD; 1. PE 1: Evidence at protein level; KW 3D-structure; Dioxygenase; Direct protein sequencing; Iron; KW Metal-binding; Oxidoreductase; Phenylalanine catabolism; KW Tyrosine catabolism. FT CHAIN 1 357 4-hydroxyphenylpyruvate dioxygenase. FT /FTId=PRO_0000088408. FT COMPBIAS 167 196 Tyr-rich. FT METAL 161 161 Iron. FT METAL 240 240 Iron. FT METAL 322 322 Iron. FT STRAND 10 19 FT HELIX 27 32 FT STRAND 36 51 FT STRAND 54 59 FT STRAND 62 64 FT HELIX 65 73 FT STRAND 74 85 FT HELIX 87 96 FT STRAND 115 117 FT HELIX 119 121 FT STRAND 123 127 FT STRAND 131 133 FT HELIX 136 140 FT STRAND 141 143 FT STRAND 155 162 FT HELIX 170 182 FT STRAND 185 193 FT STRAND 198 205 FT STRAND 212 218 FT HELIX 225 233 FT STRAND 235 237 FT STRAND 240 246 FT HELIX 248 257 FT HELIX 268 272 FT HELIX 274 277 FT HELIX 285 291 FT STRAND 294 300 FT STRAND 303 312 FT STRAND 319 328 FT HELIX 334 351 SQ SEQUENCE 357 AA; 40061 MW; 26CF4A80B1484BD0 CRC64; ADLYENPMGL MGFEFIELAS PTPNTLEPIF EIMGFTKVAT HRSKDVHLYR QGAINLILNN EPHSVASYFA AEHGPSVCGM AFRVKDSQKA YKRALELGAQ PIHIETGPME LNLPAIKGIG GAPLYLIDRF GEGSSIYDID FVFLEGVDRH PVGAGLKIID HLTHNVYRGR MAYWANFYEK LFNFREIRYF DIKGEYTGLT SKAMTAPDGM IRIPLNEESS KGAGQIEEFL MQFNGEGIQH VAFLSDDLIK TWDHLKSIGM RFMTAPPDTY YEMLEGRLPN HGEPVGELQA RGILLDGSSE SGDKRLLLQI FSETLMGPVF FEFIQRKGDD GFGEGNFKAL FESIERDQVR RGVLSTD //